BISPECIFIC ANTIBODY MODIFICATION OF NICOTINIC ACETYLCHOLINE-RECEPTORSFOR BIOSENSING

Recent results show that bispecific antibodies can be used to tailor t he selectivity of nicotinic acetylcholine receptors for biosensing pur poses. The nicotinic acetylcholine receptors reconstituted in bilayer lipid membranes are inactivated when two bispecific antibodies, attach ed to the same receptor, bind to a single antigen molecule. Experiment s with patch clamp recording equipment reveal that antigen levels of 1 0(-8) M completely and irreversibly inactivate small numbers of nicoti nic acetylcholine receptors. This approach may lead to the constructio n of biosensors capable of detecting individual antibody-antigen (Ab-A g) binding events.